Immobilization of enzymes by bioaffinity layering

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Abstract

Bioaffinity immobilization exploits the affinity of the enzyme to a macro-(affinity ligand). Such a macro-(affinity ligand) could be a lectin, a water-soluble polymer, or a bioconjugate of a water-soluble polymer and the appropriate affinity ligand. Successive layering of the enzyme and the macro-(affinity ligand) on a matrix allows deposition of a large amount of enzyme activity on a small surface. Illustrative protocols show affinity layering of a pectinase and horseradish peroxidase on Concanavalin A-agarose and Concanavalin A-Sephadex matrices, respectively. © Springer Science+Business Media, New York 2013.

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Singh, V., Sardar, M., & Gupta, M. N. (2013). Immobilization of enzymes by bioaffinity layering. Methods in Molecular Biology, 1051, 129–137. https://doi.org/10.1007/978-1-62703-550-7_9

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